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P0A6F5 (CH60_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60 kDa chaperonin
Alternative name(s):
GroEL protein
Protein Cpn60
Gene names
Name:groL
Synonyms:groEL, mopA
Ordered Locus Names:b4143, JW4103
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. HAMAP-Rule MF_00600

Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell. HAMAP-Rule MF_00600

Subunit structure

Oligomer of 14 subunits composed of two stacked rings of 7 subunits.

Subcellular location

Cytoplasm. Note: Uniformly located in the cytoplasm (Ref.15). Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase (Ref.17); polar localization depends on the minCDE operon. Foci form near midcell Probable. Ref.15 Ref.17

Post-translational modification

Phosphorylated reversibly during heat shock. Ref.11

Miscellaneous

This protein shows ATPase activity.

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Caution

Was originally (Ref.6) designated as the ams protein.

Sequence caution

The sequence AAA23934.1 differs from that shown. Reason: Frameshift at positions 424 and 455.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 379350. Source: GOC

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from mutant phenotype PubMed 2573517. Source: EcoCyc

protein refolding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

response to heat

Inferred from expression pattern PubMed 8349564. Source: EcoliWiki

virion assembly

Inferred from mutant phenotype PubMed 7015340. Source: EcoliWiki

   Cellular_componentcytosol

Inferred from direct assay PubMed 16858726. Source: UniProtKB

membrane

Inferred from direct assay PubMed 16858726. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.22. Source: EcoCyc

ATPase activity

Inferred from direct assay PubMed 379350. Source: EcoCyc

identical protein binding

Inferred from physical interaction PubMed 16858726PubMed 22575645PubMed 8618836PubMed 9878052. Source: IntAct

protein binding

Inferred from physical interaction PubMed 10077571PubMed 11779463PubMed 12071968PubMed 14517228PubMed 15313620PubMed 15690043PubMed 16239229PubMed 16606699PubMed 16977315PubMed 18394994PubMed 18418386PubMed 20959808PubMed 23746846PubMed 24561554PubMed 8618836Ref.22PubMed 9878052. Source: IntAct

unfolded protein binding

Inferred from mutant phenotype PubMed 2573517. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 54854760 kDa chaperonin HAMAP-Rule MF_00600
PRO_0000063358

Amino acid modifications

Modified residue341N6-succinyllysine Ref.16
Modified residue511N6-succinyllysine Ref.16
Modified residue1171N6-acetyllysine; alternate Ref.14
Modified residue1171N6-succinyllysine; alternate Ref.16
Modified residue2771N6-succinyllysine Ref.16
Modified residue3211N6-succinyllysine Ref.16
Modified residue3901N6-succinyllysine Ref.16

Experimental info

Sequence conflict83 – 864DAAG → GALQ in CAA30739. Ref.5
Sequence conflict2621L → A in CAA30698. Ref.1
Sequence conflict2671M → I in CAA30698. Ref.1
Sequence conflict3431Q → R in AAA23934. Ref.6

Secondary structure

.......................................................................................... 548
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6F5 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: CD3A0FB505F74AD1

FASTA54857,329
        10         20         30         40         50         60 
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI 

        70         80         90        100        110        120 
ELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGI 

       130        140        150        160        170        180 
DKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDG 

       190        200        210        220        230        240 
TGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAV 

       250        260        270        280        290        300 
AKAGKPLLII AEDVEGEALA TLVVNTMRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTV 

       310        320        330        340        350        360 
ISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDY 

       370        380        390        400        410        420 
DREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALI 

       430        440        450        460        470        480 
RVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNA 

       490        500        510        520        530        540 
ATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG 


MGGMGGMM 

« Hide

References

« Hide 'large scale' references
[1]"Homologous plant and bacterial proteins chaperone oligomeric protein assembly."
Hemmingsen S.M., Woolford C., van der Vies S.M., Tilly K., Dennis D.T., Georgopoulos C., Hendrix R.W., Ellis R.J.
Nature 333:330-334(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Control of cell division by sex factor F in Escherichia coli. III. Participation of the groES (mopB) gene of the host bacteria."
Miki T., Orita T., Furuno M., Horiuchi T.
J. Mol. Biol. 201:327-338(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86.
[6]"Cloning, sequence analysis, and expression of alteration of the mRNA stability gene (ams+) of Escherichia coli."
Chanda P.K., Ono M., Kuwano M., Kung H.-F.
J. Bacteriol. 161:446-449(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-495.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22.
Strain: K12 / EMG2.
[8]Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.
Submitted (FEB-1996) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]"A role of RnlA in the RNase LS activity from Escherichia coli."
Otsuka Y., Koga M., Iwamoto A., Yonesaki T.
Genes Genet. Syst. 82:291-299(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 4-10.
Strain: K12.
[10]"The reaction of GroEL (cpn 60) with the ATP analogue 2',3' dialdehyde ATP."
Thomson G.J., Coggins J.R., Price N.C.
FEBS Lett. 336:19-22(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 455-519.
[11]"Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation."
Sherman M.Y., Goldberg A.L.
Nature 357:167-169(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[12]"Residues in chaperonin GroEL required for polypeptide binding and release."
Fenton W.A., Kashi Y., Furtak K., Horwich A.L.
Nature 371:614-619(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[13]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[14]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[15]"Quantitative and spatio-temporal features of protein aggregation in Escherichia coli and consequences on protein quality control and cellular ageing."
Winkler J., Seybert A., Konig L., Pruggnaller S., Haselmann U., Sourjik V., Weiss M., Frangakis A.S., Mogk A., Bukau B.
EMBO J. 29:910-923(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[16]"Identification of lysine succinylation as a new post-translational modification."
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION AT LYS-34; LYS-51; LYS-117; LYS-277; LYS-321 AND LYS-390.
Strain: K12.
[17]"Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli."
Li G., Young K.D.
Mol. Microbiol. 84:276-295(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[18]"The crystal structure of the bacterial chaperonin GroEL at 2.8 A."
Braig K., Otwinowski Z., Hegde R.S., Boisvert D.C., Joachimiak A., Horwich A.L., Sigler P.B.
Nature 371:578-586(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[19]"Conformational variability in the refined structure of the chaperonin GroEL at 2.8-A resolution."
Braig K., Adams P.D., Bruenger A.T.
Nat. Struct. Biol. 2:1083-1094(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[20]"The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S."
Boisvert D.C., Wang J., Otwinowski Z., Horwich A.L., Sigler P.B.
Nat. Struct. Biol. 3:170-177(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[21]"Chaperone activity and structure of monomeric polypeptide binding domains of GroEL."
Zahn R., Buckle A.M., Perrett S., Johnson C.M., Corrales F.J., Golbik R., Fersht A.R.
Proc. Natl. Acad. Sci. U.S.A. 93:15024-15029(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[22]"The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex."
Xu Z., Horwich A.L., Sigler P.B.
Nature 388:741-750(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[23]"The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity."
Chen L., Sigler P.B.
Cell 99:757-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 192-337.
[24]"Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions."
Kiser P.D., Lodowski D.T., Palczewski K.
Acta Crystallogr. F 63:457-461(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07850 Genomic DNA. Translation: CAA30698.1.
U14003 Genomic DNA. Translation: AAA97042.1.
U00096 Genomic DNA. Translation: AAC77103.1.
AP009048 Genomic DNA. Translation: BAE78145.1.
X07899 Genomic DNA. Translation: CAA30739.1.
M11294 Genomic DNA. Translation: AAA23934.1. Frameshift.
PIRBVECGL. S56371.
RefSeqNP_418567.1. NC_000913.3.
YP_492286.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AONX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1DK7X-ray2.02A/B191-336[»]
1DKDX-ray2.10A/B/C/D191-336[»]
1FY9X-ray2.20A191-376[»]
1FYAX-ray2.20A191-376[»]
1GR5electron microscopy7.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1GRLX-ray2.80A/B/C/D/E/F/G1-548[»]
1GRUelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1J4ZX-ray3.52A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1JONX-ray2.50A191-345[»]
1KIDX-ray1.70A188-376[»]
1KP8X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1KPOX-ray3.521/2/O/P/Q/R/S/T/U/V/W/X/Y/Z2-548[»]
1LA1X-ray2.06A188-379[»]
1MNFX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
1OELX-ray2.80A/B/C/D/E/F/G2-548[»]
1PCQX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1PF9X-ray2.99A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1SS8X-ray2.70A/B/C/D/E/F/G2-525[»]
1SVTX-ray2.81A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1SX3X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-526[»]
1SX4X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
1XCKX-ray2.92A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Celectron microscopy7.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Delectron microscopy8.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2C7Eelectron microscopy9.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2CGTelectron microscopy8.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2EU1X-ray3.29A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
2NWCX-ray3.02A/B/C/D/E/F/G/H/I/J/K/L/M/N2-548[»]
2YEYX-ray3.30A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
3C9Velectron microscopy4.70A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3CAUelectron microscopy4.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3VZ6X-ray1.50A191-376[»]
3VZ7X-ray1.80A191-376[»]
3VZ8X-ray1.90A/B/C191-376[»]
3ZPZelectron microscopy8.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
3ZQ0electron microscopy9.20A/B/C/D/E/F/G/H/I/J/K/L/M/N2-525[»]
3ZQ1electron microscopy15.90A/B/C/D/E/F/G/H/I/J/K/L/M/N2-527[»]
4AAQelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AARelectron microscopy8.00A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AASelectron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AAUelectron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AB2electron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
4AB3electron microscopy8.50A/B/C/D/E/F/G/H/I/J/K/L/M/N1-548[»]
ProteinModelPortalP0A6F5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852957. 1 interaction.
DIPDIP-339N.
IntActP0A6F5. 697 interactions.
MINTMINT-5232496.
STRING511145.b4143.

2D gel databases

SWISS-2DPAGEP0A6F5.

Proteomic databases

PaxDbP0A6F5.
PRIDEP0A6F5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77103; AAC77103; b4143.
BAE78145; BAE78145; BAE78145.
GeneID12934083.
948665.
KEGGecj:Y75_p4030.
eco:b4143.
PATRIC32123855. VBIEscCol129921_4275.

Organism-specific databases

EchoBASEEB0594.
EcoGeneEG10599. groL.

Phylogenomic databases

eggNOGCOG0459.
HOGENOMHOG000076290.
KOK04077.
OMAVLFGNDA.
OrthoDBEOG6JDWBZ.
PhylomeDBP0A6F5.

Enzyme and pathway databases

BioCycEcoCyc:EG10599-MONOMER.
ECOL316407:JW4103-MONOMER.
SABIO-RKP0A6F5.

Gene expression databases

GenevestigatorP0A6F5.

Family and domain databases

Gene3D1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPMF_00600. CH60.
InterProIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PANTHERPTHR11353. PTHR11353. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00298. CHAPERONIN60.
SUPFAMSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsTIGR02348. GroEL. 1 hit.
PROSITEPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A6F5.
PROP0A6F5.

Entry information

Entry nameCH60_ECOLI
AccessionPrimary (citable) accession number: P0A6F5
Secondary accession number(s): P06139, Q2M6G1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene